HEY1_HUMAN - dbPTM
HEY1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HEY1_HUMAN
UniProt AC Q9Y5J3
Protein Name Hairy/enhancer-of-split related with YRPW motif protein 1
Gene Name HEY1
Organism Homo sapiens (Human).
Sequence Length 304
Subcellular Localization Nucleus .
Protein Description Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGTG-3'. [PubMed: 11095750 Downstream effector of Notch signaling required for cardiovascular development. Specifically required for the Notch-induced endocardial epithelial to mesenchymal transition, which is itself criticial for cardiac valve and septum development. May be required in conjunction with HEY2 to specify arterial cell fate or identity. Promotes maintenance of neuronal precursor cells and glial versus neuronal fate specification. Represses transcription by the cardiac transcriptional activators GATA4 and GATA6 and by the neuronal bHLH factors ASCL1/MASH1 and NEUROD4/MATH3]
Protein Sequence MKRAHPEYSSSDSELDETIEVEKESADENGNLSSALGSMSPTTSSQILARKRRRGIIEKRRRDRINNSLSELRRLVPSAFEKQGSAKLEKAEILQMTVDHLKMLHTAGGKGYFDAHALAMDYRSLGFRECLAEVARYLSIIEGLDASDPLRVRLVSHLNNYASQREAASGAHAGLGHIPWGTVFGHHPHIAHPLLLPQNGHGNAGTTASPTEPHHQGRLGSAHPEAPALRAPPSGSLGPVLPVVTSASKLSPPLLSSVASLSAFPFSFGSFHLLSPNALSPSAPTQAANLGKPYRPWGTEIGAF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
8PhosphorylationMKRAHPEYSSSDSEL
CCCCCCCCCCCCHHH
20.5020363803
9PhosphorylationKRAHPEYSSSDSELD
CCCCCCCCCCCHHHH
23.0020363803
10PhosphorylationRAHPEYSSSDSELDE
CCCCCCCCCCHHHHH
36.9420363803
11PhosphorylationAHPEYSSSDSELDET
CCCCCCCCCHHHHHC
38.9320363803
13PhosphorylationPEYSSSDSELDETIE
CCCCCCCHHHHHCEE
41.8420363803
25PhosphorylationTIEVEKESADENGNL
CEEEEHHHCCCCCCH
52.6819413330
34PhosphorylationDENGNLSSALGSMSP
CCCCCHHHHHHCCCC
30.5822210691
38PhosphorylationNLSSALGSMSPTTSS
CHHHHHHCCCCCCHH
19.5522210691
40PhosphorylationSSALGSMSPTTSSQI
HHHHHCCCCCCHHHH
22.3128348404
42PhosphorylationALGSMSPTTSSQILA
HHHCCCCCCHHHHHH
31.8129449344
43PhosphorylationLGSMSPTTSSQILAR
HHCCCCCCHHHHHHH
29.7529449344
44PhosphorylationGSMSPTTSSQILARK
HCCCCCCHHHHHHHH
23.7929449344
45PhosphorylationSMSPTTSSQILARKR
CCCCCCHHHHHHHHH
21.1022210691
59AcetylationRRRGIIEKRRRDRIN
HHCCHHHHHHHHHHH
40.5730589147
78PhosphorylationELRRLVPSAFEKQGS
HHHHHCHHHHHHHCC
37.8024719451
97PhosphorylationKAEILQMTVDHLKML
HHHHHHHHHHHHHHH
15.15-
161PhosphorylationLVSHLNNYASQREAA
HHHHHHHHHHHHHHH
13.4223911959
163PhosphorylationSHLNNYASQREAASG
HHHHHHHHHHHHHCC
21.2923911959

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseORF50O92608
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HEY1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of HEY1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYOD1_HUMANMYOD1physical
11279181
NOTC1_HUMANNOTCH1genetic
18239137
SE1L1_HUMANSEL1Lphysical
24366871
SYVN1_HUMANSYVN1physical
24366871
HEY2_HUMANHEY2physical
24366871
DERL2_HUMANDERL2physical
24366871
HES1_HUMANHES1physical
26068074
MYCB2_HUMANMYCBP2physical
26068074
FBSP1_HUMANFBXO45physical
26068074
SKP1_HUMANSKP1physical
26068074
DPF3_HUMANDPF3physical
26582913
TLE1_HUMANTLE1physical
19321451
HEY1_HUMANHEY1physical
19802006
HES1_HUMANHES1physical
19802006
HEY2_HUMANHEY2physical
19802006
HES1_HUMANHES1physical
27129302
HEY2_HUMANHEY2physical
27129302
P53_HUMANTP53physical
27129302
STK38_HUMANSTK38physical
27129302
ST38L_HUMANSTK38Lphysical
27129302
RL11_HUMANRPL11physical
27129302
MDM2_HUMANMDM2physical
27129302
NONO_HUMANNONOphysical
27129302
CSK2B_HUMANCSNK2Bphysical
27129302
MARK3_HUMANMARK3physical
27129302
TBA1B_HUMANTUBA1Bphysical
27129302
TBB4B_HUMANTUBB4Bphysical
27129302
TBA1A_HUMANTUBA1Aphysical
27129302
TBB2A_HUMANTUBB2Aphysical
27129302
TBB5_HUMANTUBBphysical
27129302
TBB3_HUMANTUBB3physical
27129302
TBA4A_HUMANTUBA4Aphysical
27129302
TBB4A_HUMANTUBB4Aphysical
27129302
FLNA_HUMANFLNAphysical
27129302
ACTB_HUMANACTBphysical
27129302
VIME_HUMANVIMphysical
27129302
HSP7C_HUMANHSPA8physical
27129302
GRP78_HUMANHSPA5physical
27129302
HS90B_HUMANHSP90AB1physical
27129302
TCPE_HUMANCCT5physical
27129302
TCPZ_HUMANCCT6Aphysical
27129302
TCPQ_HUMANCCT8physical
27129302
CCD78_HUMANCCDC78physical
27129302
GRDN_HUMANCCDC88Aphysical
27129302
CC124_HUMANCCDC124physical
27129302
TMA7_HUMANTMA7physical
27129302
TITIN_HUMANTTNphysical
27129302
SYNE1_HUMANSYNE1physical
27129302
SYNE2_HUMANSYNE2physical
27129302
TNKS1_HUMANTNKSphysical
27129302
TB182_HUMANTNKS1BP1physical
27129302
AKAP9_HUMANAKAP9physical
27129302
TERA_HUMANVCPphysical
27129302
PLEC_HUMANPLECphysical
27129302
EWS_HUMANEWSR1physical
27129302
CSK21_HUMANCSNK2A1physical
27129302
M18BP_HUMANMIS18BP1physical
27129302
PTN13_HUMANPTPN13physical
27129302
RAB1A_HUMANRAB1Aphysical
27129302
APC_HUMANAPCphysical
27129302
DCTN1_HUMANDCTN1physical
27129302
FMNL1_HUMANFMNL1physical
27129302
CDC6_HUMANCDC6physical
27129302
BIRC6_HUMANBIRC6physical
27129302
PAF15_HUMANKIAA0101physical
27129302
RL8_HUMANRPL8physical
27129302
RS10_HUMANRPS10physical
27129302
RS25_HUMANRPS25physical
27129302
HNRPK_HUMANHNRNPKphysical
27129302
RS19_HUMANRPS19physical
27129302
RS7_HUMANRPS7physical
27129302
RL15_HUMANRPL15physical
27129302
RS16_HUMANRPS16physical
27129302
RS18_HUMANRPS18physical
27129302
RL12_HUMANRPL12physical
27129302
RS14_HUMANRPS14physical
27129302
RL23_HUMANRPL23physical
27129302
RS3_HUMANRPS3physical
27129302
RS29_HUMANRPS29physical
27129302
RS20_HUMANRPS20physical
27129302
RL9_HUMANRPL9physical
27129302
ROA1_HUMANHNRNPA1physical
27129302
SMD1_HUMANSNRPD1physical
27129302
SMD3_HUMANSNRPD3physical
27129302
RL22L_HUMANRPL22L1physical
27129302
RSMB_HUMANSNRPBphysical
27129302
RS17_HUMANRPS17physical
27129302
SNR27_HUMANSNRNP27physical
27129302
RS5_HUMANRPS5physical
27129302
UBIM_HUMANFAUphysical
27129302
HNRH1_HUMANHNRNPH1physical
27129302
RS15A_HUMANRPS15Aphysical
27129302
HNRLL_HUMANHNRNPLLphysical
27129302
HNRPD_HUMANHNRNPDphysical
27129302
ROA2_HUMANHNRNPA2B1physical
27129302
FRG1_HUMANFRG1physical
27129302
FEN1_HUMANFEN1physical
27129302
FBRL_HUMANFBLphysical
27129302
DDX5_HUMANDDX5physical
27129302
NOLC1_HUMANNOLC1physical
27129302
YLPM1_HUMANYLPM1physical
27129302
YBOX1_HUMANYBX1physical
27129302
EZRI_HUMANEZRphysical
27129302
DDX46_HUMANDDX46physical
27129302
IQEC1_HUMANIQSEC1physical
27129302

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HEY1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-45, AND MASSSPECTROMETRY.

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